PHO32_ARATH
ID PHO32_ARATH Reviewed; 242 AA.
AC Q8VYN9; Q9LSR2;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Universal stress protein PHOS32 {ECO:0000303|PubMed:12644671};
DE AltName: Full=Phosphorylated protein of 32 kDa {ECO:0000303|PubMed:18285339};
DE Short=AtPHOS32 {ECO:0000303|PubMed:18285339};
DE Flags: Precursor;
GN Name=PHOS32 {ECO:0000303|PubMed:18285339};
GN OrderedLocusNames=At5g54430 {ECO:0000312|Araport:AT5G54430};
GN ORFNames=F24B18.5 {ECO:0000312|EMBL:BAA97516.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:AAL49890.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION.
RX PubMed=12644671; DOI=10.1104/pp.102.016006;
RA Kerk D., Bulgrien J., Smith D.W., Gribskov M.;
RT "Arabidopsis proteins containing similarity to the universal stress protein
RT domain of bacteria.";
RL Plant Physiol. 131:1209-1219(2003).
RN [7]
RP MUTAGENESIS OF SER-21, PHOSPHORYLATION UPON BACTERIAL ELICITATION,
RP PHOSPHORYLATION AT SER-21 BY MAPK3 AND MAPK6, AND NICKEL-BINDING.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=18285339; DOI=10.1074/jbc.m800735200;
RA Merkouropoulos G., Andreasson E., Hess D., Boller T., Peck S.C.;
RT "An Arabidopsis protein phosphorylated in response to microbial
RT elicitation, AtPHOS32, is a substrate of MAP kinases 3 and 6.";
RL J. Biol. Chem. 283:10493-10499(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP PHOSPHORYLATION UPON INFECTION BY PHYTOPHTHORA INFESTANS ZOOSPORES AND
RP XYLANASE, AND PHOSPHORYLATION AT SER-21.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18785823; DOI=10.1094/mpmi-21-10-1275;
RA Lenman M., Soerensson C., Andreasson E.;
RT "Enrichment of phosphoproteins and phosphopeptide derivatization identify
RT universal stress proteins in elicitor-treated Arabidopsis.";
RL Mol. Plant Microbe Interact. 21:1275-1284(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- PTM: Phosphorylated by MAPK3 and MAPK6 after pathogenic elicitation
CC (e.g. bacterial flg22, Phytophthora infestans zoospores and xylanase).
CC {ECO:0000269|PubMed:18285339, ECO:0000269|PubMed:18785823}.
CC -!- MISCELLANEOUS: Can bind nickel. {ECO:0000269|PubMed:18285339}.
CC -!- SIMILARITY: Belongs to the universal stress protein A family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97516.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026634; BAA97516.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96495.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70952.1; -; Genomic_DNA.
DR EMBL; AK118526; BAC43129.1; -; mRNA.
DR EMBL; AY070394; AAL49890.1; -; mRNA.
DR EMBL; AY123025; AAM67558.1; -; mRNA.
DR EMBL; AY087680; AAM65217.1; -; mRNA.
DR RefSeq; NP_001332519.1; NM_001345084.1.
DR RefSeq; NP_001332520.1; NM_001345085.1.
DR RefSeq; NP_001332521.1; NM_001345082.1.
DR RefSeq; NP_568808.1; NM_124823.4.
DR AlphaFoldDB; Q8VYN9; -.
DR SMR; Q8VYN9; -.
DR STRING; 3702.AT5G54430.1; -.
DR iPTMnet; Q8VYN9; -.
DR PaxDb; Q8VYN9; -.
DR PRIDE; Q8VYN9; -.
DR ProteomicsDB; 236154; -.
DR EnsemblPlants; AT5G54430.1; AT5G54430.1; AT5G54430.
DR EnsemblPlants; AT5G54430.4; AT5G54430.4; AT5G54430.
DR GeneID; 835531; -.
DR Gramene; AT5G54430.1; AT5G54430.1; AT5G54430.
DR Gramene; AT5G54430.4; AT5G54430.4; AT5G54430.
DR KEGG; ath:AT5G54430; -.
DR Araport; AT5G54430; -.
DR TAIR; locus:2147319; AT5G54430.
DR eggNOG; ENOG502RXH2; Eukaryota.
DR HOGENOM; CLU_049301_0_0_1; -.
DR InParanoid; Q8VYN9; -.
DR OMA; HEHIKDG; -.
DR PhylomeDB; Q8VYN9; -.
DR PRO; PR:Q8VYN9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYN9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002238; P:response to molecule of fungal origin; IDA:TAIR.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR044162; PHOS32/34.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR006015; Universal_stress_UspA.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR31966; PTHR31966; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR01438; UNVRSLSTRESS.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Nucleotide-binding; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..242
FT /note="Universal stress protein PHOS32"
FT /id="PRO_0000436334"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT BINDING 168..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT BINDING 186..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q57997"
FT MOD_RES 21
FT /note="Phosphoserine; by MAPK3 and MAPK6"
FT /evidence="ECO:0000269|PubMed:18285339,
FT ECO:0000269|PubMed:18785823, ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MUTAGEN 21
FT /note="S->A,D: Impaired phosphorylation by MAPK3 and
FT MAPK6."
FT /evidence="ECO:0000269|PubMed:18285339"
SQ SEQUENCE 242 AA; 26202 MW; AB31B159CDAF3EA9 CRC64;
MNPADSDHPQ LPNIKIHHPP SPRHSHHHHS SSTPSSAATP TPTAGARRKI GVAVDLSEES
SFAVRWAVDH YIRPGDAVVL LHVSPTSVLF GADWGPLPLK TQIEDPNAQP QPSQEDFDAF
TSTKVADLAK PLKELGFPYK IHIVKDHDMR ERLCLEIERL GLSAVIMGSR GFGAEKKRGS
DGKLGSVSDY CVHHCVCPVV VVRYPDDRDG PVPIVTVKSG GDDDGDVVAA SASAHHEHIK
DE
